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CAZyme Information: MGYG000001013_00371

You are here: Home > Sequence: MGYG000001013_00371

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Ezakiella sp900540185
Lineage Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Ezakiella; Ezakiella sp900540185
CAZyme ID MGYG000001013_00371
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
372 MGYG000001013_2|CGC1 40700.86 6.3734
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001013 1653935 MAG Bangladesh Asia
Gene Location Start: 152960;  End: 154078  Strand: +

Full Sequence      Download help

MLLKNAAVFI  GGKYKRKDLW  IEDGKIKFIM  DEIMADGLDL  SGKRIIPGLT  DIHTHGAMGK60
DSSDGEVGSI  ETIAKYNLEH  GITQFCPTTM  TFNEEILNGI  FKSIGEYDNK  YSEVVGIHME120
GPFISKDKIG  AQNPKYLMDP  DVGMVERLDE  KSGGLLRIIS  IAPEINGAME  FAKKLGDKYV180
LSVAHTNATY  DEAVDAFKNG  FSHLTHTFNA  MPGIHHRKPG  VIPAAIENGS  TAELITDGVH240
IHDAIIRLIF  KLFGNTRMIL  VSDSNEATGL  SDGEYMLGGQ  KIVKVKNKAT  IKGTDTIAGS300
ATNLFDCMKH  AIKAGIKEED  AIRAATINPA  KLLGIDRRVG  TIREGNVANL  LVLDDELNIE360
RIFLRGEEIC  KK372

Enzyme Prediction      help

No EC number prediction in MGYG000001013_00371.

CAZyme Signature Domains help

Created with Snap18375574931111301481671862042232412602792973163343534366CE9
Family Start End Evalue family coverage
CE9 4 366 1.2e-117 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap18375574931111301481671862042232412602792973163343531366NagA1369NagA2366nagA21368nagA45358Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.15e-130 1 366 1 374
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
COG1820 NagA 1.10e-110 1 369 2 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.05e-83 2 366 6 379
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 3.32e-58 21 368 23 378
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.09e-28 45 358 2 313
Amidohydrolase family. This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyzes adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.

CAZyme Hits      help

Created with Snap18375574931111301481671862042232412602792973163343531369AVM67637.1|CE91366QOS67292.1|CE91367CBL07941.1|CE91367VCV23836.1|CE91369AYA99755.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
AVM67637.1 7.35e-116 1 369 1 368
QOS67292.1 9.31e-114 1 366 1 370
CBL07941.1 1.05e-111 1 367 1 376
VCV23836.1 2.97e-111 1 367 1 376
AYA99755.1 3.28e-111 1 369 1 379

PDB Hits      download full data without filtering help

Created with Snap183755749311113014816718620422324126027929731633435313662VHL_A53677NUT_A383673EGJ_A213676FV3_A213676FV4_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 5.63e-59 1 366 5 384
TheThree-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis],2VHL_B The Three-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis]
7NUT_A 5.96e-58 5 367 17 399
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUT_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_A Chain A, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens]
3EGJ_A 8.49e-53 38 367 47 377
N-acetylglucosamine-6-phosphatedeacetylase from Vibrio cholerae. [Vibrio cholerae],3EGJ_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae. [Vibrio cholerae],3IV8_A N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_C N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_D N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae]
6FV3_A 1.45e-51 21 367 31 390
Crystalstructure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_B Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_C Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_D Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155]
6FV4_A 2.15e-50 21 367 31 390
Thestructure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155],6FV4_B The structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits      download full data without filtering help

Created with Snap18375574931111301481671862042232412602792973163343535372sp|Q6P0U0|NAGA_DANRE1366sp|O34450|NAGA_BACSU5367sp|A7MBC0|NAGA_BOVIN5367sp|Q9Y303|NAGA_HUMAN1366sp|Q84F86|NAGA_LYSSH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q6P0U0 9.76e-63 5 372 17 404
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
O34450 3.08e-58 1 366 5 384
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0 8.40e-58 5 367 17 399
N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q9Y303 3.27e-57 5 367 17 399
N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
Q84F86 6.11e-55 1 366 6 379
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001013_00371.